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一种单克隆免疫球蛋白G冷球蛋白的动力学和结构特性研究。

Study of the kinetic and structural properties of a monoclonal immunoglobulin G cryoglobulin.

作者信息

Scoville C D, Turner D H, Lippert J L, Abraham G N

出版信息

J Biol Chem. 1980 Jun 25;255(12):5847-52.

PMID:7380838
Abstract

The precipitation of a monoclonal IgG2 crystalline cryoglobulin (WEB) is shown to occur via a nucleation mechanism. The kinetics of precipitation fits the empirical equation 1n(t2/t1) = nù(c1/c2), where t is the time to reach half-maximum turbidity for concentration c. The effect of mild reduction of interchain disulfides on the kinetics and extent of precipitation have also been determined. Cleavage of only one or two inter heavy-heavy chain disulfide bonds appears to abolish cryoprecipitation. The extent of reduction at high reductant levels suggests that there is an extra inter heavy-heavy chain disulfide in IgG-WEB. Laser Raman spectroscopy detects no structural change between reduced (noncryoprecipitable) and native (cryoprecipitable) WEB, suggesting that perturbation of a local site is responsible for loss of cryoprecipitation.

摘要

一种单克隆IgG2结晶冷球蛋白(WEB)的沉淀通过成核机制发生。沉淀动力学符合经验方程ln(t2/t1) = ν(c1/c2),其中t是浓度为c时达到最大浊度一半所需的时间。还确定了链间二硫键轻度还原对沉淀动力学和程度的影响。仅切割一两个重链间二硫键似乎就会消除冷沉淀。高还原剂水平下的还原程度表明IgG-WEB中存在额外的重链间二硫键。激光拉曼光谱未检测到还原型(不可冷沉淀)和天然型(可冷沉淀)WEB之间的结构变化,这表明局部位点的扰动是冷沉淀丧失的原因。

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